ID A0A091DKJ1_FUKDA Unreviewed; 1204 AA.
AC A0A091DKJ1;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 40.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN ORFNames=H920_07883 {ECO:0000313|EMBL:KFO30780.1};
OS Fukomys damarensis (Damaraland mole rat) (Cryptomys damarensis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Bathyergidae;
OC Fukomys.
OX NCBI_TaxID=885580 {ECO:0000313|EMBL:KFO30780.1, ECO:0000313|Proteomes:UP000028990};
RN [1] {ECO:0000313|EMBL:KFO30780.1, ECO:0000313|Proteomes:UP000028990}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Liver {ECO:0000313|EMBL:KFO30780.1};
RA Gladyshev V.N., Fang X.;
RT "The Damaraland mole rat (Fukomys damarensis) genome and evolution of
RT African mole rats.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27; Evidence={ECO:0000256|ARBA:ARBA00000900};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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DR EMBL; KN122382; KFO30780.1; -; Genomic_DNA.
DR RefSeq; XP_010628458.1; XM_010630156.1.
DR AlphaFoldDB; A0A091DKJ1; -.
DR STRING; 885580.ENSFDAP00000006083; -.
DR GeneID; 104866269; -.
DR CTD; 9666; -.
DR eggNOG; KOG0800; Eukaryota.
DR OrthoDB; 5256194at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000028990; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:InterPro.
DR GO; GO:0000209; P:protein polyubiquitination; IEA:InterPro.
DR CDD; cd16460; RING-H2_DZIP3; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR033103; DZIP3_RING-H2_finger.
DR InterPro; IPR041249; HEPN_DZIP3.
DR InterPro; IPR043866; TTC3/DZIP3_dom.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR15727:SF4; E3 UBIQUITIN-PROTEIN LIGASE DZIP3; 1.
DR PANTHER; PTHR15727; RING FINGER PROTEIN 214; 1.
DR Pfam; PF18738; HEPN_DZIP3; 1.
DR Pfam; PF19179; TTC3_DZIP3_dom; 1.
DR Pfam; PF13639; zf-RING_2; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000028990};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 1144..1184
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 1..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 636..713
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1085..1135
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 776..849
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..16
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 25..40
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 669..691
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1085..1131
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1204 AA; 137847 MW; 6F438CCFDE793949 CRC64;
MDSLPEEFFV REAAVEDQNE EETENEVEKS AIQPDKQKKD IPTDLVPGDL LLEVKKLLNA
INTLPKGVVP HIKKFLQEDF CFQTMQREVA ASSQNGEEVV PALTLRFLIT QLETALRNIQ
ATNYTAYQID IGYYLTLLFL YGVSLTERGK KEDYTEAENK FLVMKMVIQE NEICENFMSL
VYFGRGLLRC AQKRYNGGLL EFHKSLQEIG DINDHWFDID PTEDEDLPTN FKDLLNSFIK
TTENNIMKQT ICSYLDCERS CEADILKNTN YKGFFQLMCS KNCCIYFHKI CWKKFKNLKY
PGENDQSFSG KTCLKEGCTG DMVRMLQGDV PGTVKILFEV VRKDECITIE NLGASYKKLM
SLKIADTDIR PKIGLKFNTK DEMPIFKLDY NYFYHLLHII IISGTDIVRQ IFDEAMPPPL
LKKELLIHKN VLESYYNHLW TNHPLGGSWH LLYPPNKELP QSKQFDLCLL LALIKHLNVF
PAPQKGWIME PPSSDLSKSA DILRLCKYRD ILLSEILMNG LTESQFNSIW KKVSDILLRL
GMKQEDIDKV KENPIENISL DYHQLSIYLG IPVPEIIQRM LSCYQQGIAL QSITGSQRIE
IEELQNEEED LSPPLMEYNI NVKSNSELQL ADMNKDGASI PSESSTESVK DLQEVKSKPK
KKKTTKHKKS KDSKEEKISY MREKEEQLKN EQTNPHPMGR FMKDDAGDQE DSATEDKFYS
LDELHILDMI EQGSTGKVTT DCGETEKERL VQQQLYKLHY RCEDFKKQLK TMIFRCQENQ
MQIKKKEKII ASLNQQVTFG INKVSKLQRQ VHAKDNEIKN FKEQFSMKRS QWEMEKHNLE
STIKTYLNKL NAETSRALTA EVYFLQCRRD FGLLHLEQTE KECLSQLARV THMAASSLES
LQLKAAVDSW NSIVADVRNK IAVLRTQYNE QINKVKQGFP LSSLPPIQLP PPPPSPELLM
QQYLGRPIVK DSFFRPILTV PQMPAICPAV ISAPGQPRPP LMTGIAWTMP TPVGETVPPS
AGLGTDLSLM NWERITDRLK TAFPQQTRKE LTDFLLKLKE AHGKSLSGLT CDEIVYKISQ
FIDPKKPQSQ EKTVPNGNVS PSDSSSQTNA PQPPKSAWSS LSSQGSATWE EANNVDEEEE
EEPCVICHEN LSPENLSVLP CAHKFHSQCI RPWLMQQGTC PTCRLHVLLP EEFPGHTSQQ
LPKV
//